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Title: Novel localization of formin mDia2: importin ?-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope
Authors: Shao, X 
Kawauchi, K 
Shivashankar, G.V 
Bershadsky, A.D 
Keywords: 4 amino 6 [2 [[4 (diethylamino) 1 methylbutyl]amino] 6 methyl 4 pyrimidinyl] 2 methylquinoline
calcium ion
diaphanous related formin 1
diaphanous related formin 3
F actin
guanosine triphosphatase
inverted formin 2
karyopherin beta
lamin b1
Nup153 protein
Rac1 protein
unclassified drug
actin polymerization
amino terminal sequence
cell function
cell nucleus membrane
cellular distribution
controlled study
gene silencing
human cell
nuclear localization signal
nuclear pore complex
protein interaction
sequence analysis
Issue Date: 2015
Citation: Shao, X, Kawauchi, K, Shivashankar, G.V, Bershadsky, A.D (2015). Novel localization of formin mDia2: importin ?-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope. Biology Open 4 (11) : 1569-1575. ScholarBank@NUS Repository.
Abstract: The formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations. Here, we show that Diaphanous-related formin-3 (mDia2) localizes to the cytoplasmic side of the nuclear envelope. This localization of mDia2 to the nuclear rim required the presence of a nuclear localization signal (NLS) sequence at the mDia2 N-terminal. Consistent with this result, super-resolution images demonstrated that at the nuclear rim, mDia2 co-localized with the nuclear pore complexes and a nuclear transport receptor, importin β. Furthermore, an interaction between mDia2 and importin β was detected by immunoprecipitation, and silencing of importin β was shown to attenuate accumulation of mDia2 to the nuclear rim. We have shown previously that Ca2+ entry leads to the assembly of perinuclear actin rim in an inverted formin 2 (INF2) dependent manner. mDia2, however, was not involved in this process since abolishing its localization at the nuclear rim by silencing of importin β had no effect on actin assembly at the nuclear rim triggered by Ca2+ stimulation. © 2015. Published by The Company of Biologists Ltd.
Source Title: Biology Open
ISSN: 2046-6390
DOI: 10.1242/bio.013649
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